1izc
From Proteopedia
(New page: 200px<br /><applet load="1izc" size="450" color="white" frame="true" align="right" spinBox="true" caption="1izc, resolution 1.7Å" /> '''Crystal Structure Ana...) |
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| - | [[Image:1izc.jpg|left|200px]]<br /><applet load="1izc" size=" | + | [[Image:1izc.jpg|left|200px]]<br /><applet load="1izc" size="350" color="white" frame="true" align="right" spinBox="true" |
caption="1izc, resolution 1.7Å" /> | caption="1izc, resolution 1.7Å" /> | ||
'''Crystal Structure Analysis of Macrophomate synthase'''<br /> | '''Crystal Structure Analysis of Macrophomate synthase'''<br /> | ||
==Overview== | ==Overview== | ||
| - | The Diels-Alder reaction, which forms a six-membered ring from an alkene | + | The Diels-Alder reaction, which forms a six-membered ring from an alkene (dienophile) and a 1,3-diene, is synthetically very useful for construction of cyclic products with high regio- and stereoselectivity under mild conditions. It has been applied to the synthesis of complex pharmaceutical and biologically active compounds. Although evidence on natural Diels-Alderases has been accumulated in the biosynthesis of secondary metabolites, there has been no report on the structural details of the natural Diels-Alderases. The function and catalytic mechanism of the natural Diels-Alderase are of great interest owing to the diversity of molecular skeletons in natural Diels-Alder adducts. Here we present the 1.70 A resolution crystal structure of the natural Diels-Alderase, fungal macrophomate synthase (MPS), in complex with pyruvate. The active site of the enzyme is large and hydrophobic, contributing amino acid residues that can hydrogen-bond to the substrate 2-pyrone. These data provide information on the catalytic mechanism of MPS, and suggest that the reaction proceeds via a large-scale structural reorganization of the product. |
==About this Structure== | ==About this Structure== | ||
| - | 1IZC is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Macrophoma_commelinae Macrophoma commelinae] with MG and PYR as [http://en.wikipedia.org/wiki/ligands ligands]. Full crystallographic information is available from [http:// | + | 1IZC is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Macrophoma_commelinae Macrophoma commelinae] with <scene name='pdbligand=MG:'>MG</scene> and <scene name='pdbligand=PYR:'>PYR</scene> as [http://en.wikipedia.org/wiki/ligands ligands]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1IZC OCA]. |
==Reference== | ==Reference== | ||
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[[Category: tim-barrel]] | [[Category: tim-barrel]] | ||
| - | ''Page seeded by [http:// | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 13:17:21 2008'' |
Revision as of 11:17, 21 February 2008
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Crystal Structure Analysis of Macrophomate synthase
Overview
The Diels-Alder reaction, which forms a six-membered ring from an alkene (dienophile) and a 1,3-diene, is synthetically very useful for construction of cyclic products with high regio- and stereoselectivity under mild conditions. It has been applied to the synthesis of complex pharmaceutical and biologically active compounds. Although evidence on natural Diels-Alderases has been accumulated in the biosynthesis of secondary metabolites, there has been no report on the structural details of the natural Diels-Alderases. The function and catalytic mechanism of the natural Diels-Alderase are of great interest owing to the diversity of molecular skeletons in natural Diels-Alder adducts. Here we present the 1.70 A resolution crystal structure of the natural Diels-Alderase, fungal macrophomate synthase (MPS), in complex with pyruvate. The active site of the enzyme is large and hydrophobic, contributing amino acid residues that can hydrogen-bond to the substrate 2-pyrone. These data provide information on the catalytic mechanism of MPS, and suggest that the reaction proceeds via a large-scale structural reorganization of the product.
About this Structure
1IZC is a Single protein structure of sequence from Macrophoma commelinae with and as ligands. Full crystallographic information is available from OCA.
Reference
Insight into a natural Diels-Alder reaction from the structure of macrophomate synthase., Ose T, Watanabe K, Mie T, Honma M, Watanabe H, Yao M, Oikawa H, Tanaka I, Nature. 2003 Mar 13;422(6928):185-9. PMID:12634789
Page seeded by OCA on Thu Feb 21 13:17:21 2008
Categories: Macrophoma commelinae | Single protein | Honma, M. | Mie, T. | Oikawa, H. | Ose, T. | Tanaka, I. | Watanabe, H. | Watanabe, K. | Yao, M. | MG | PYR | Pyruvate mg(ii) complex | Tim-barrel
